期刊
NUCLEIC ACIDS RESEARCH
卷 45, 期 8, 页码 4866-4880出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkw1365
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资金
- National Research Foundation of Korea (NRF) - Korea government (MSIP) [20110021713, 2015R1A2A2A04005596]
- R&D Convergence Program of NST (National Research Council of Science & Technology) of Republic of Korea [CAP-16-03-KRIBB]
- National Research Foundation of Korea [2015R1A2A2A04005596] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Post-translational modifications contribute to the spliceosome dynamics by facilitating the physical re-arrangements of the spliceosome. Here, we report USP15, a deubiquitinating enzyme, as a regulator of protein-protein interactions for the spliceosome dynamics. We show that PRP31, a component of U4 snRNP, is modified with K63-linked ubiquitin chains by the PRP19 complex and deubiquitinated by USP15 and its substrate targeting factor SART3. USP15(SART3) makes a complex with USP4 and this ternary complex serves as a platform to deubiquitinate PRP31 and PRP3. The ubiquitination and deubiquitination status of PRP31 regulates its interaction with the U5 snRNP component PRP8, which is required for the efficient splicing of chromosome segregation related genes, probably by stabilizing the U4/U6. U5 tri-snRNP complex. Collectively, our data suggest that USP15 plays a key role in the regulation of dynamic protein-protein interactions of the spliceosome.
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